Coomassie Blue R-250 (Highly Pure) – Catalog Number: B2012364 (5 g)

Coomassie Blue R-250 (Highly Pure) is a widely used triphenylmethane dye (about 826 g/mol) supplied here as a biotechnology-grade powder (5 g; Catalog B2012364) with storage recommended at −20 °C. Celebrated for its robust blue coloration, this dye remains a cornerstone in protein biochemistry for visualizing and quantifying proteins, as well as for monitoring chromatographic processes or serving as a visible tracer in electrophoresis workflows.

In biochemical laboratories, Coomassie Blue R-250 is central to SDS-PAGE staining—binding proteins through aromatic and basic amino acid residues and producing a stable color shift that enhances visibility. Its high affinity for protein residues enables detection of low-microgram quantities, making it indispensable in polyacrylamide gel analysis, Bradford assays, and dye-binding quantitations. Additionally, its defined chemical and physical profile makes it well suited for calibration curves, performance benchmarking, and validating gel consistency.

Researchers leverage its robustness in method development, especially when precision and repeatability are critical. Reconstituting this powder in acidic, aqueous buffers allows creation of reliable working stocks. Application specificity includes colorimetric quantitation, protein aggregation monitoring, and visualizing protein integrity. The consistent purity and formulation facilitate integration into automated imaging, densitometry platforms, and reproducible SOPs, while the −20 °C storage aids in long-term dye stability.

Why researchers choose this product:

• Highly pure powder (5 g) ensures reproducibility in staining and quantitation workflows
• 826 g/mol composition allows precise molecular referencing and documentation
• Standard staining dye for SDS-PAGE and Bradford protein assays
• Reliable blue chromophore enables sensitive visual detection of protein bands
• Cold storage enhances shelf-life and assay consistency

This product is for Research Use Only (RUO). It is not intended for diagnostic or therapeutic use.

References

• 1: Kumar G. Fungal Laccase Efficiently Destains Coomassie Brilliant Blue-R-250 Stained Polyacrylamide Gels Methods Mol Biol. 2018;1853:247-253.
• 2: Nagata K, Ashikaga R, Mori W, Zako T, Shimazaki Y. Analysis of the enzymatic degradation of lysozyme fibrils using a combination method of non-denaturing gel electrophoresis and double staining with Coomassie Brilliant Blue G-250 and R-250 dyes Anal Sci. 2022 Nov 30.
• 3: Yang J, Yang X, Ye X, Lin J. Destaining of Coomassie Brilliant Blue R_250-stained polyacrylamide gels with fungal laccase Anal Biochem. 2016 Jan 15;493:27-9.
• 4: Yang J, Yang X, Ye X, Lin J. Optimal parameters for laccase-mediated destaining of Coomassie Brilliant Blue R_250-stained polyacrylamide gels Data Brief. 2016 Jan 29;7:1-7.
• 5: Goldring JPD. The Roles of Acetic Acid and Methanol During Fixing and Staining Proteins in an SDS-Polyacrylamide Electrophoresis Gel Methods Mol Biol. 2018;1853:15-18.
• 6: Hu PP, Liu H, Zhan L, Zheng LL, Huang CZ. Coomassie brilliant blue R_250 as a new surface-enhanced Raman scattering probe for prion protein through a dual-aptamer mechanism Talanta. 2015 Jul 1;139:35-9.
• 7: Hattori S, Sakai K, Watanabe K, Fujii T. The induction of metachromasia and circular dichroism of coomassie brilliant blue R_250 with collagen and histone H1 is due to the low content of hydrophobic amino acid residues in these proteins J Biochem. 1996 Mar;119(3):400-6.
• 8: Rosenthal HL, Berger RA, Tyler AN, Moore BW. Isolation of a component from commercial coomassie brilliant blue R_250 that stains rubrophilin and other proteins red on polyacrylamide gels Biochim Biophys Acta. 1988 May 12;965(2-3):432-40.
• 9: Duhamel RC, Meezan E, Brendel K. Metachromatic staining with Coomassie Brilliant Blue R_250 of the proline-rich calf thymus histone, H1 Biochim Biophys Acta. 1980 Dec 16;626(2):432-42.
• 10: Sreeramulu G, Singh NK. Destaining of Coomassie Brilliant Blue R-250-stained polyacrylamide gels with sodium chloride solutions Electrophoresis. 1995 Mar;16(3):362-5.